What is it about?
Protein-RNA recognition, often govern by the conformational flexibility of the binding partners, plays important roles in cellular processes. This article provides a dataset of protein-RNA complex structures and the corresponding unbound structures of the binding partners, i.e. protein and RNA curated from the Protein Data Bank.
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Why is it important?
This benchmark dataset can provide a fundamental understanding on the change in conformational flexibility upon binding in both protein and RNA. Furthermore, it can be used to benchmark the flexible protein-RNA docking algorithms.
Perspectives
Binding induced conformational change is numerous in protein-RNA recognition. However, it is far to understood the structural mechanism of such recognition. The structures of bound and unbound partners may further be analyzed to understand the origin of binding induced conformational changes in protein-RNA recognition.
Ranjit Bahadur
Read the Original
This page is a summary of: A non-redundant protein-RNA docking benchmark version 2.0, Proteins Structure Function and Bioinformatics, December 2016, Wiley,
DOI: 10.1002/prot.25211.
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